癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
HSPC142 Antibody (N-term) 精选
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q9NWV8 |
| Other Accession | Q6AXK4, Q08E57, NP_054892 |
| Reactivity | Human |
| Predicted | Bovine, Zebrafish, Mouse, Rat, Canine, Chicken |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 36560 Da |
| Antigen Region | 9-37 aa |
| Gene ID | 29086 |
|---|---|
| Other Names | BRISC and BRCA1-A complex member 1, Mediator of RAP80 interactions and targeting subunit of 40 kDa, New component of the BRCA1-A complex, BABAM1, C19orf62, MERIT40, NBA1 |
| Target/Specificity | This HSPC142 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 9-37 amino acids from the N-terminal region of human HSPC142. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | HSPC142 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | BABAM1 |
|---|---|
| Function | Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'- linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). |
| Cellular Location | Cytoplasm. Nucleus Note=Localizes at sites of DNA damage at double-strand breaks (DSBs) |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
HSPC142 is a component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. HSPC142 probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. In these 2 complexes, it is probably required to maintain the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36. component
REFERENCES
Solyom, S., et al. Breast Cancer Res. Treat. 120(1):165-168(2010)
Cooper, E.M., et al. EMBO J. 28(6):621-631(2009)
Olsen, J.V., et al. Cell 127(3):635-648(2006)
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